TBB5_ORYSJ
ID TBB5_ORYSJ Reviewed; 447 AA.
AC P46265; Q0E3L8; Q6H4W0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Tubulin beta-5 chain;
DE AltName: Full=Beta-5-tubulin;
GN Name=TUBB5; Synonyms=OSTB-50, R2242, TUB5;
GN OrderedLocusNames=Os02g0167300, LOC_Os02g07060;
GN ORFNames=OsJ_05524 {ECO:0000312|EMBL:EAZ21874.1}, OSJNBa0085K21.33;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Nipponbare; TISSUE=Root;
RX PubMed=7788525; DOI=10.1093/dnares/2.1.21;
RA Koga-Ban Y., Niki T., Nagamura Y., Sasaki T., Minobe Y.;
RT "cDNA sequences of three kinds of beta-tubulins from rice.";
RL DNA Res. 2:21-26(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Arborio; TISSUE=Coleoptile;
RX PubMed=7610170; DOI=10.1104/pp.108.2.823;
RA Breviario D., Giani S., Meoni C.;
RT "Three rice cDNA clones encoding different beta-tubulin isotypes.";
RL Plant Physiol. 108:823-824(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 1-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=cv. Nipponbare;
RX PubMed=16758443; DOI=10.1002/pmic.200600043;
RA Nozu Y., Tsugita A., Kamijo K.;
RT "Proteomic analysis of rice leaf, stem and root tissues during growth
RT course.";
RL Proteomics 6:3665-3670(2006).
RN [9]
RP TISSUE SPECIFICITY, INDUCTION, AND NOMENCLATURE.
RX PubMed=14634157; DOI=10.1093/pcp/pcg150;
RA Yoshikawa M., Yang G., Kawaguchi K., Komatsu S.;
RT "Expression analyses of beta-tubulin isotype genes in rice.";
RL Plant Cell Physiol. 44:1202-1207(2003).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC hollow water-filled tube with an outer diameter of 25 nm and an inner
CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC form protofilaments running lengthwise along the microtubule wall with
CC the beta-tubulin subunit facing the microtubule plus end conferring a
CC structural polarity. Microtubules usually have 13 protofilaments but
CC different protofilament numbers can be found in some organisms and
CC specialized cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaf sheaths, and suspension
CC cultured cells. {ECO:0000269|PubMed:14634157}.
CC -!- INDUCTION: By gibberellin and brassinolide. Down-regulated by abscisic
CC acid (ABA). {ECO:0000269|PubMed:14634157, ECO:0000269|PubMed:7788525}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; D30717; BAA06382.1; -; mRNA.
DR EMBL; X79367; CAA55912.1; -; mRNA.
DR EMBL; AP005804; BAD26239.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07920.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77161.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ21874.1; -; Genomic_DNA.
DR EMBL; AK121574; BAH00558.1; -; mRNA.
DR PIR; S45040; S45040.
DR RefSeq; XP_015625553.1; XM_015770067.1.
DR AlphaFoldDB; P46265; -.
DR SMR; P46265; -.
DR BioGRID; 797457; 1.
DR STRING; 4530.OS02T0167300-01; -.
DR PaxDb; P46265; -.
DR PRIDE; P46265; -.
DR EnsemblPlants; Os02t0167300-01; Os02t0167300-01; Os02g0167300.
DR GeneID; 4328420; -.
DR Gramene; Os02t0167300-01; Os02t0167300-01; Os02g0167300.
DR KEGG; osa:4328420; -.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P46265; -.
DR OMA; VCSVAPK; -.
DR OrthoDB; 962471at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; P46265; baseline and differential.
DR Genevisible; P46265; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW Microtubule; Nucleotide-binding; Reference proteome.
FT CHAIN 1..447
FT /note="Tubulin beta-5 chain"
FT /id="PRO_0000048367"
FT REGION 421..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 154
FT /note="K -> M (in Ref. 2; CAA55912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50105 MW; 54241ACF0C58A564 CRC64;
MREILHIQGG QCGNQIGAKF WEVICDEHGI DHTGKYSGDS DLQLERINVY YNEASGGRFV
PRAVLMDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVLDVV
RKEAENCDCL QGFQVCHSLG GGTGSGMGTL LISKIREEYP DRMMLTFSVF PSPKVSDTVV
EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLATP TFGDLNHLIS ATMSGVTCCL
RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YRALTVPELT QQMWDAKNMM
CAADPRHGRY LTASAMFRGK MSTKEVDEQM LNVQNKNSSY FVEWIPNNVK SSVCDIPPNG
LKMASTFIGN STSIQEMFRR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVA
EYQQYQDATA DDEEEDYGDE EEDEVAA
